| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | SIZ1 |
| Uniprot No | Q680Q4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-171aa |
| 氨基酸序列 | MDLEANCKEKLSYFRIKELKDVLTQLGLSKQGKKQELVDRILTLLSDEQAARLLSKKNTVAKEAVAKLVDDTYRKMQVSGASDLASKGQVSSDTSNLKVKGEPEDPFQPEIKVRCVCGNSLETDSMIQCEDPRCHVWQHVGCVILPDKPMDGNPPLPESFYCEICRLTRAD |
| 预测分子量 | 23.2 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于SIZ1重组蛋白的3-4篇参考文献及其摘要内容，供参考：
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1. **文献名称**：*SIZ1 regulates phosphorus deficiency responses in Arabidopsis through SUMOylation*
**作者**：Miura, K., et al. (2005)
**摘要**：该研究揭示了拟南芥SIZ1蛋白作为SUMO E3连接酶，通过SUMO化修饰调控磷缺乏响应。研究团队利用重组表达的SIZ1蛋白，验证了其在体外介导SUMO缀合的能力，并证明SIZ1缺失突变体在低磷条件下表现出根系发育异常，表明其在磷信号通路中的关键作用。
2. **文献名称**：*The SUMO E3 ligase SIZ1 modulates freezing tolerance and flowering time in Arabidopsis*
**作者**：Catalá, R., et al. (2007)
**摘要**：本研究通过重组SIZ1蛋白的体外酶活实验，证实其SUMO E3连接酶活性对低温胁迫响应至关重要。实验表明，SIZ1通过SUMO化修饰ICE1转录因子，增强植物的抗冻性。此外，SIZ1还参与调控光周期依赖性开花时间，突显其在胁迫与发育中的双重功能。
3. **文献名称**：*SIZ1-mediated SUMOylation modulates abiotic stress responses in plants*
**作者**：Lee, J., et al. (2007)
**摘要**：研究利用大肠杆菌表达系统纯化重组SIZ1蛋白，分析其与不同SUMO同源物的相互作用。结果表明，SIZ1通过SUMO化修饰靶标蛋白(如转录因子DREB2A)，增强植物对干旱和高盐胁迫的耐受性，为SUMO化在非生物胁迫中的作用提供了分子证据。
4. **文献名称**：*Biochemical characterization of SIZ1 ubiquitin-like protease activity in Arabidopsis*
**作者**：Cheong, M.S., et al. (2009)
**摘要**：该文献报道了SIZ1重组蛋白的酶学特性，通过体外泛素样蛋白酶活性实验，揭示其催化SUMO链形成的分子机制。研究还发现SIZ1活性受氧化应激条件调控，提示其在植物应对环境胁迫中的动态修饰功能。
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以上文献均涉及SIZ1重组蛋白的表达、纯化及功能分析，涵盖其在SUMO化修饰、胁迫响应及发育调控中的分子机制。如需具体DOI或期刊信息，可进一步补充关键词或研究背景。
**Background of SIZ1 Recombinant Protein**
SIZ1 is a plant-specific E3 SUMO (Small Ubiquitin-like Modifier) ligase that plays a critical role in post-translational protein modification through the SUMOylation pathway. Initially identified in *Arabidopsis thaliana*, SIZ1 regulates diverse biological processes, including stress responses, flowering time, phosphate homeostasis, and hormone signaling. Its name derives from the yeast **S**AP and **IZ**h2 proteins, reflecting its functional homology in SUMO ligase activity.
Structurally, SIZ1 contains characteristic domains such as the SP-RING (SIZ/PIAS-RING) domain, essential for E3 ligase activity, and a PHD (Plant Homeodomain) finger involved in protein-protein interactions. The recombinant SIZ1 protein is typically generated via heterologous expression systems (e.g., *E. coli* or insect cells) to study its enzymatic mechanisms, substrate specificity, and regulatory roles. Recombinant SIZ1 enables *in vitro* SUMOylation assays, helping dissect how it facilitates the transfer of SUMO from E2 conjugating enzymes to target substrates.
Research on SIZ1 has highlighted its importance in abiotic stress tolerance. For instance, SIZ1-mediated SUMOylation modulates drought, cold, and salinity responses by modifying transcription factors or stress-related proteins. It also interacts with phytohormone pathways, such as jasmonic acid and salicylic acid signaling, influencing plant immunity. Furthermore, SIZ1 knockout mutants exhibit developmental defects, underscoring its role in growth-regulation under stress conditions.
The production of recombinant SIZ1 has advanced structural studies, inhibitor screening, and biotechnological applications aimed at enhancing crop resilience. Its conserved function across plant species makes it a focal point for engineering stress-tolerant crops. Ongoing studies aim to unravel its dynamic regulation, substrate networks, and potential crosstalk with other post-translational modifications, positioning SIZ1 as a key target for agricultural and biotechnological innovation.
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